If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Synonyms: purine nucleotide catabolism (aerobic)
|Superclasses:||Degradation/Utilization/Assimilation → Nucleosides and Nucleotides Degradation → Purine Nucleotides Degradation|
Expected Taxonomic Range: Embryophyta
In most plants, purine nucleotides are completely degraded to CO2 and ammonia via the ureides (S)-(+)-allantoin and allantoate. This degradation proceeds via the intermediates xanthine and urate.
The initial step of AMP degradation is the conversion of AMP to IMP, which is converted to xanthine in two alternative routes, via xanthosine or hypoxanthine. The initial step of GMP degradation is the conversion of GMP to guanosine, which is also degraded to xanthine in two ways, via guanine or xanthosine.
Studies in tea leaves and cultured Catharanthus roseus cells showed that guanosine deaminase activity was much higher than that of guanine deaminase [Ashihara97]. It indicates the degradation pathway of GMP via xanthosine is likely to be the major route. Xanthine is then converted to urate by xanthine dehydrogenase [Hesberg04].
Superpathways: superpathway of purines degradation in plants
Variants: pseudouridine degradation, purine deoxyribonucleosides degradation I, purine deoxyribonucleosides degradation II, purine nucleobases degradation I (anaerobic), purine nucleobases degradation II (anaerobic), purine nucleotides degradation II (aerobic), purine ribonucleosides degradation, urate biosynthesis/inosine 5'-phosphate degradation
Unification Links: AraCyc:PWY-5044
Hesberg04: Hesberg C, Hansch R, Mendel RR, Bittner F (2004). "Tandem orientation of duplicated xanthine dehydrogenase genes from Arabidopsis thaliana: differential gene expression and enzyme activities." J Biol Chem 279(14);13547-54. PMID: 14726515
Amaya02: Amaya Y, Kawamoto S, Kashima Y, Okamoto K, Nishino T (2002). "Purification and characterization of multiple forms of rat liver xanthine oxidoreductase expressed in baculovirus-insect cell system." J Biochem 132(4);597-606. PMID: 12359075
Asai07: Asai R, Matsumura T, Okamoto K, Igarashi K, Pai EF, Nishino T (2007). "Two mutations convert mammalian xanthine oxidoreductase to highly superoxide-productive xanthine oxidase." J Biochem 141(4);525-34. PMID: 17301076
BauschJurken95: Bausch-Jurken MT, Sabina RL (1995). "Divergent N-terminal regions in AMP deaminase and isoform-specific catalytic properties of the enzyme." Arch Biochem Biophys 321(2);372-80. PMID: 7646062
Dutka04: Dutka P, Szydlowska M, Chodorowski Z, Rybakowska I, Nagel-Starczynowska G, Kaletha K (2004). "AMP-deaminase from normal and cirrhotic human liver: a comparative study." Mol Cell Biochem 262(1-2);119-26. PMID: 15532716
Elshafei95: Elshafei AM, Abu-Shady MR, el-Beih FM, Mohamed LA (1995). "Mode and extent of degradation of adenosine and guanosine by extracts of Aspergillus terricola." Microbiol Res 150(3);291-5. PMID: 7551735
Gilbert79: Gilbert HJ, Lowe CR, Drabble WT (1979). "Inosine 5'-monophosphate dehydrogenase of Escherichia coli. Purification by affinity chromatography, subunit structure and inhibition by guanosine 5'-monophosphate." Biochem J 1979;183(3);481-94. PMID: 44191
Hager95: Hager PW, Collart FR, Huberman E, Mitchell BS (1995). "Recombinant human inosine monophosphate dehydrogenase type I and type II proteins. Purification and characterization of inhibitor binding." Biochem Pharmacol 49(9);1323-9. PMID: 7763314
Itoh03: Itoh R, Saint-Marc C, Chaignepain S, Katahira R, Schmitter JM, Daignan-Fornier B (2003). "The yeast ISN1 (YOR155c) gene encodes a new type of IMP-specific 5'-nucleotidase." BMC Biochem 4;4. PMID: 12735798
Jung09: Jung B, Florchinger M, Kunz HH, Traub M, Wartenberg R, Jeblick W, Neuhaus HE, Mohlmann T (2009). "Uridine-ribohydrolase is a key regulator in the uridine degradation pathway of Arabidopsis." Plant Cell 21(3);876-91. PMID: 19293370
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